Issue 46, 2015
From the journal:

Chemical Communications

Cisplatin binding to human serum albumin: a structural study†

Giarita Ferraro,a   Lara Massai,b   Luigi Messorib  and  Antonello Merlino*ac  

* Corresponding authors

a Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, Napoli, Italy
E-mail: antonello.merlino@unina.it
Fax: +39 081674090
Tel: +39 081674276

b Department of Chemistry, University of Florence, Via della Lastruccia 3, I-50019 Sesto Fiorentino, FI, Italy

c CNR Institute of Biostructures and Bioimages, Via Mezzocannone 16, Napoli, Italy

Abstract

The reaction between cisplatin and human serum albumin (HSA) was investigated by X-ray crystallography and crystal structures of the cisplatin/HSA adduct were eventually solved for the first time. Structural data unambiguously prove that cisplatin mainly binds to His105 and Met329 side chains; additional binding sites are detected at His288, Met298, and Met548 and at His535, His67 and His247.

Graphical abstract: Cisplatin binding to human serum albumin: a structural study

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Article information

DOI
https://doi.org/10.1039/C5CC01751C
Article type
Communication
Submitted
28 Feb 2015
Accepted
08 Apr 2015
First published
08 Apr 2015

Chem. Commun., 2015,51, 9436-9439

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Cisplatin binding to human serum albumin: a structural study

G. Ferraro, L. Massai, L. Messori and A. Merlino, Chem. Commun., 2015, 51, 9436 DOI: 10.1039/C5CC01751C

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